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Volumn 160, Issue , 2008, Pages 159-171

Exploring the uremic toxins using proteomic technologies

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; TOXIN;

EID: 48949093788     PISSN: 03025144     EISSN: None     Source Type: Book Series    
DOI: 10.1159/000125973     Document Type: Review
Times cited : (16)

References (65)
  • 1
    • 0032838784 scopus 로고    scopus 로고
    • Pathophysiologic effects of uremic retention solutes
    • Vanholder R, De Smet R: Pathophysiologic effects of uremic retention solutes. J Am Soc Nephrol 1999;10:1815-1823.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 1815-1823
    • Vanholder, R.1    De Smet, R.2
  • 3
    • 0037406406 scopus 로고    scopus 로고
    • Review on uremic toxins: Classification, concentration, and interindividual variability
    • Vanholder R, De Smet R, Glorieux G, Argiles, et al: Review on uremic toxins: classification, concentration, and interindividual variability. Kidney Int 2003;63:1934-1943.
    • (2003) Kidney Int , vol.63 , pp. 1934-1943
    • Vanholder, R.1    De Smet, R.2    Glorieux, G.3    Argiles4
  • 4
  • 5
    • 32944477687 scopus 로고    scopus 로고
    • Effects of oral vitamin C supplementation in hemodialysis patients: A proteomic assessment
    • Weissinger EM, Nguyen-Khoa T, Fumeron C, Saltiel C, et al: Effects of oral vitamin C supplementation in hemodialysis patients: a proteomic assessment. Proteomics 2006;6:993-1000.
    • (2006) Proteomics , vol.6 , pp. 993-1000
    • Weissinger, E.M.1    Nguyen-Khoa, T.2    Fumeron, C.3    Saltiel, C.4
  • 6
    • 4043094133 scopus 로고    scopus 로고
    • Proteomics in nephrology: Current status and future directions
    • Thongboonkerd V: Proteomics in nephrology: current status and future directions. Am J Nephrol 2004;24:360-378.
    • (2004) Am J Nephrol , vol.24 , pp. 360-378
    • Thongboonkerd, V.1
  • 7
    • 0016711037 scopus 로고
    • High-resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH: High-resolution two-dimensional electrophoresis of proteins. J Biol Chem 1975;250:4007-4021.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 8
    • 0028824080 scopus 로고
    • Mass spectrometric approaches for the identification of gel-separated proteins
    • Patterson SD, Aebersold R: Mass spectrometric approaches for the identification of gel-separated proteins. Electrophoresis 1995;16:1791-1814.
    • (1995) Electrophoresis , vol.16 , pp. 1791-1814
    • Patterson, S.D.1    Aebersold, R.2
  • 9
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold R, Goodlett DR: Mass spectrometry in proteomics. Chem Rev 2001;101:269-295.
    • (2001) Chem Rev , vol.101 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 11
    • 0034772403 scopus 로고    scopus 로고
    • The role of separation science in proteomics research
    • Issaq HJ: The role of separation science in proteomics research. Electrophoresis 2001;22:3629-3638.
    • (2001) Electrophoresis , vol.22 , pp. 3629-3638
    • Issaq, H.J.1
  • 14
    • 16344384394 scopus 로고    scopus 로고
    • Renal and urinary proteomics: Current applications and challenges
    • Thongboonkerd V, Malasit P: Renal and urinary proteomics: current applications and challenges. Proteomics 2005;5:1033-1042.
    • (2005) Proteomics , vol.5 , pp. 1033-1042
    • Thongboonkerd, V.1    Malasit, P.2
  • 15
    • 0042736304 scopus 로고    scopus 로고
    • Rapid discovery and identification of a tissue-specific tumor biomarker from 39 human cancer cell lines using the SELDI ProteinChip platform
    • Shiwa M, Nishimura Y, Wakatabe R, Fukawa A, et al: Rapid discovery and identification of a tissue-specific tumor biomarker from 39 human cancer cell lines using the SELDI ProteinChip platform. Biochem Biophys Res Commun 2003;309:18-25.
    • (2003) Biochem Biophys Res Commun , vol.309 , pp. 18-25
    • Shiwa, M.1    Nishimura, Y.2    Wakatabe, R.3    Fukawa, A.4
  • 16
    • 0036079692 scopus 로고    scopus 로고
    • The SELDI-TOF MS approach to proteomics: Protein profiling and biomarker identification
    • Issaq HJ, Veenstra TD, Conrads TP, Felschow D: The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification. Biochem Biophys Res Commun 2002;292: 587-592.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 587-592
    • Issaq, H.J.1    Veenstra, T.D.2    Conrads, T.P.3    Felschow, D.4
  • 17
    • 0036295754 scopus 로고    scopus 로고
    • A rapid method to capture and screen for transcription factors by SELDI mass spectrometry
    • Forde CE, Gonzales AD, Smessaert JM, Murphy GA, et al: A rapid method to capture and screen for transcription factors by SELDI mass spectrometry. Biochem Biophys Res Commun 2002;290:1328-1335.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1328-1335
    • Forde, C.E.1    Gonzales, A.D.2    Smessaert, J.M.3    Murphy, G.A.4
  • 18
    • 0038561093 scopus 로고    scopus 로고
    • SELDI ProteinChip array in oncoproteomic research
    • Yip TT, Lomas L: SELDI ProteinChip array in oncoproteomic research. Technol Cancer Res Treat 2002;1:273-280.
    • (2002) Technol Cancer Res Treat , vol.1 , pp. 273-280
    • Yip, T.T.1    Lomas, L.2
  • 19
    • 0034013944 scopus 로고    scopus 로고
    • Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry
    • Merchant M, Weinberger SR: Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis 2000;21:1164-1177.
    • (2000) Electrophoresis , vol.21 , pp. 1164-1177
    • Merchant, M.1    Weinberger, S.R.2
  • 20
    • 0034852859 scopus 로고    scopus 로고
    • Mass spectrometry meets chip technology: A new proteomic tool in cancer research?
    • Von Eggeling F, Junker K, Fiedle W, Wollscheid V, et al: Mass spectrometry meets chip technology: a new proteomic tool in cancer research? Electrophoresis 2001;22:2898-2902.
    • (2001) Electrophoresis , vol.22 , pp. 2898-2902
    • Von Eggeling, F.1    Junker, K.2    Fiedle, W.3    Wollscheid, V.4
  • 21
    • 0036079692 scopus 로고    scopus 로고
    • The SELDI-TOF MS approach to proteomics: Protein profiling and biomarker identification
    • Issaq HJ, Veenstra TD, Conrads TP, Felschow D: The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification. Biochem Biophys Res Commun 2002;292:587-592.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 587-592
    • Issaq, H.J.1    Veenstra, T.D.2    Conrads, T.P.3    Felschow, D.4
  • 22
    • 0036748438 scopus 로고    scopus 로고
    • Tagless extraction-retentate chromatography: A new global protein digestion strategy for monitoring differential protein expression
    • Weinberger SR, Viner RI, Ho P: Tagless extraction-retentate chromatography: a new global protein digestion strategy for monitoring differential protein expression. Electrophoresis 2002;23:3182-3192.
    • (2002) Electrophoresis , vol.23 , pp. 3182-3192
    • Weinberger, S.R.1    Viner, R.I.2    Ho, P.3
  • 24
    • 0037116832 scopus 로고    scopus 로고
    • Use of proteomic patter ns in serum to identify ovarian cancer
    • Petricoin EF, Ardekani AM, Hitt BA, Levine PJ, et al: Use of proteomic patter ns in serum to identify ovarian cancer. Lancet 2002;359:572-577.
    • (2002) Lancet , vol.359 , pp. 572-577
    • Petricoin, E.F.1    Ardekani, A.M.2    Hitt, B.A.3    Levine, P.J.4
  • 26
    • 0346101481 scopus 로고    scopus 로고
    • Urine protein profiling with surface-enhanced laser-desorption/ionization time-of-flight mass spectrometry
    • Schaub S, Wilkins J, Weiler T, Sangster K, et al: Urine protein profiling with surface-enhanced laser-desorption/ionization time-of-flight mass spectrometry. Kidney Int 2004;65:323-332.
    • (2004) Kidney Int , vol.65 , pp. 323-332
    • Schaub, S.1    Wilkins, J.2    Weiler, T.3    Sangster, K.4
  • 28
    • 13844316757 scopus 로고    scopus 로고
    • Signal in noise: Evaluating reported reproducibility of serum proteomic tests for ovarian cancer
    • Baggerly KA, Morris JS, Edmonson SR, Coombes KR: Signal in noise: evaluating reported reproducibility of serum proteomic tests for ovarian cancer. J Natl Cancer Inst 2005;97:307-309.
    • (2005) J Natl Cancer Inst , vol.97 , pp. 307-309
    • Baggerly, K.A.1    Morris, J.S.2    Edmonson, S.R.3    Coombes, K.R.4
  • 29
    • 1842559788 scopus 로고    scopus 로고
    • Reproducibility of SELDI-TOF protein patterns in serum: Comparing datasets from different experiments
    • Baggerly KA, Morris JS, Coombes KR: Reproducibility of SELDI-TOF protein patterns in serum: comparing datasets from different experiments Bioinformatics 2002;20:777-785.
    • (2002) Bioinformatics , vol.20 , pp. 777-785
    • Baggerly, K.A.1    Morris, J.S.2    Coombes, K.R.3
  • 30
    • 2942535913 scopus 로고    scopus 로고
    • Running before we can walk
    • Check E: Running before we can walk. Nature 2004;429:496-497.
    • (2004) Nature , vol.429 , pp. 496-497
    • Check, E.1
  • 31
    • 28044447188 scopus 로고    scopus 로고
    • Oral cancer plasma tumor marker identified with bead-based affinity-fractionated proteomic technology
    • Cheng AJ, Chen LC, Chien KY, Chen YJ, et al: Oral cancer plasma tumor marker identified with bead-based affinity-fractionated proteomic technology. Clin Chem 2005;51;2236-2244.
    • (2005) Clin Chem , vol.51 , pp. 2236-2244
    • Cheng, A.J.1    Chen, L.C.2    Chien, K.Y.3    Chen, Y.J.4
  • 32
    • 32144462497 scopus 로고    scopus 로고
    • Differential detection of S100A8 in transitional cell carcinoma of the bladder by pairwise tissue proteomic and immunohistochemical analysis
    • Tolson JP, Flad T, Gnau V, Dihazi H, et al: Differential detection of S100A8 in transitional cell carcinoma of the bladder by pairwise tissue proteomic and immunohistochemical analysis. Proteomics 2006;6:697-708.
    • (2006) Proteomics , vol.6 , pp. 697-708
    • Tolson, J.P.1    Flad, T.2    Gnau, V.3    Dihazi, H.4
  • 33
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold Rl, Mann M: Mass spectrometry-based proteomics. Nature 2003;422:198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 35
    • 0036745679 scopus 로고    scopus 로고
    • Methods for fractionation, separation and profiling of proteins and peptides
    • Issaq HJ, Conrads TP, Janini GM, Veenstra TD: Methods for fractionation, separation and profiling of proteins and peptides. Electrophoresis 2002;23:3048-3061.
    • (2002) Electrophoresis , vol.23 , pp. 3048-3061
    • Issaq, H.J.1    Conrads, T.P.2    Janini, G.M.3    Veenstra, T.D.4
  • 36
    • 31644438577 scopus 로고    scopus 로고
    • Large-scale protein profiling by combination of protein fractionation and multidimensional protein identification technology (MudPIT)
    • Chen EI, Hewel J, Felding-Habermann B, Yates JR III: Large-scale protein profiling by combination of protein fractionation and multidimensional protein identification technology (MudPIT). Mol Cell Proteomics 2006;5:53-56.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 53-56
    • Chen, E.I.1    Hewel, J.2    Felding-Habermann, B.3    Yates III, J.R.4
  • 37
    • 26844564069 scopus 로고    scopus 로고
    • Human tissue prof iling with multidimensional protein identification technology
    • Cagney G, Park S, Chung C, Tong B, et al: Human tissue prof iling with multidimensional protein identification technology. J Proteome Res 2005;4:1757-1767.
    • (2005) J Proteome Res , vol.4 , pp. 1757-1767
    • Cagney, G.1    Park, S.2    Chung, C.3    Tong, B.4
  • 38
    • 0035215402 scopus 로고    scopus 로고
    • Capillary electrophoresis of proteins 1999-2001
    • Dolnik V, Hutterer KM: Capillary electrophoresis of proteins 1999-2001. Electrophoresis 2001; 22: 4163-4178.
    • (2001) Electrophoresis , vol.22 , pp. 4163-4178
    • Dolnik, V.1    Hutterer, K.M.2
  • 39
    • 0347719602 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry: 15 years of developments and applications
    • Schmitt-Kopplin P, Frommberger M: Capillary electrophoresis-mass spectrometry: 15 years of developments and applications. Electrophoresis 2003;24:3837-3867.
    • (2003) Electrophoresis , vol.24 , pp. 3837-3867
    • Schmitt-Kopplin, P.1    Frommberger, M.2
  • 40
    • 31844431888 scopus 로고    scopus 로고
    • Recent developments in capillary electrophoresis and capillary electrochromatography of peptides
    • Kasicka V: Recent developments in capillary electrophoresis and capillary electrochromatography of peptides. Electrophoresis 2006;27:142-175.
    • (2006) Electrophoresis , vol.27 , pp. 142-175
    • Kasicka, V.1
  • 41
    • 18444393438 scopus 로고    scopus 로고
    • Combining capillary electrophoresis with mass spectrometry for applications in proteomics
    • Simpson DC, Smith RD: Combining capillary electrophoresis with mass spectrometry for applications in proteomics. Electrophoresis 2005;26:1291-1305.
    • (2005) Electrophoresis , vol.26 , pp. 1291-1305
    • Simpson, D.C.1    Smith, R.D.2
  • 42
    • 31844454314 scopus 로고    scopus 로고
    • Capillary electrophoresis of proteins 2003-2005
    • Dolnik V: Capillary electrophoresis of proteins 2003-2005. Electrophoresis 2006;27:126-141.
    • (2006) Electrophoresis , vol.27 , pp. 126-141
    • Dolnik, V.1
  • 43
    • 1642444271 scopus 로고    scopus 로고
    • Monomer surface modifications for rapid peptide analysis by capillary electrophoresis and capillary electrochromatography coupled to electrospray ionization-mass spectrometry
    • Johannesson N, Wetterhall M, Markides KE, Bergquist J: Monomer surface modifications for rapid peptide analysis by capillary electrophoresis and capillary electrochromatography coupled to electrospray ionization-mass spectrometry. Electrophoresis 2004;25:809-816.
    • (2004) Electrophoresis , vol.25 , pp. 809-816
    • Johannesson, N.1    Wetterhall, M.2    Markides, K.E.3    Bergquist, J.4
  • 44
    • 18844370547 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery
    • Kolch W, Neususs C, Pelzing M, Mischak H: Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery. Mass Spectrom Rev 2005;24:959-977.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 959-977
    • Kolch, W.1    Neususs, C.2    Pelzing, M.3    Mischak, H.4
  • 45
    • 4344690824 scopus 로고    scopus 로고
    • On-line capillary electrophoresis-mass spectrometry for the analysis of biomolecules
    • Hernandez-Borges J, Neususs C, Cifuentes A, Pelzing M: On-line capillary electrophoresis-mass spectrometry for the analysis of biomolecules. Electrophoresis 2004;25:2257-2281.
    • (2004) Electrophoresis , vol.25 , pp. 2257-2281
    • Hernandez-Borges, J.1    Neususs, C.2    Cifuentes, A.3    Pelzing, M.4
  • 46
    • 0036749373 scopus 로고    scopus 로고
    • A robust approach for the analysis of peptides in the low femtomole range by capillary electrophoresis-tandem mass spectrometry
    • Neususs C, Pelzing M, Macht M: A robust approach for the analysis of peptides in the low femtomole range by capillary electrophoresis-tandem mass spectrometry. Electrophoresis 2002;23:3149-3159.
    • (2002) Electrophoresis , vol.23 , pp. 3149-3159
    • Neususs, C.1    Pelzing, M.2    Macht, M.3
  • 47
    • 33750364830 scopus 로고    scopus 로고
    • The human urinary proteome contains more than 1,500 proteins including a large proportion of membranes proteins
    • Adachi J, Kumar C, Zhang Y, Olsen JV, Mann M: The human urinary proteome contains more than 1,500 proteins including a large proportion of membranes proteins. Genome Biol 2006;7:R80.
    • (2006) Genome Biol , vol.7
    • Adachi, J.1    Kumar, C.2    Zhang, Y.3    Olsen, J.V.4    Mann, M.5
  • 48
    • 0036523822 scopus 로고    scopus 로고
    • Off-line coupling of high-resolution capillary electrophoresis to MALDI-TOF and TOF/TOF MS
    • Rejtar T, Hu P, Juhasz P, Campbell JM, et al: Off-line coupling of high-resolution capillary electrophoresis to MALDI-TOF and TOF/TOF MS. J Proteome Res 2002;1:171-179.
    • (2002) J Proteome Res , vol.1 , pp. 171-179
    • Rejtar, T.1    Hu, P.2    Juhasz, P.3    Campbell, J.M.4
  • 49
    • 3142557616 scopus 로고    scopus 로고
    • Proteomics applied to the clinical follow-up of patients after allogeneic hematopoietic stem cell transplantation
    • Kaiser T, Kamal H, Rank A, Kolb HJ, et al: Proteomics applied to the clinical follow-up of patients after allogeneic hematopoietic stem cell transplantation. Blood 2004;104:340-349.
    • (2004) Blood , vol.104 , pp. 340-349
    • Kaiser, T.1    Kamal, H.2    Rank, A.3    Kolb, H.J.4
  • 50
    • 8644277000 scopus 로고    scopus 로고
    • Proteomic analysis for the assessment of diabetic renal damage in humans
    • Mischak H, Kaiser T, Walden M, Hillmann M, et al: Proteomic analysis for the assessment of diabetic renal damage in humans. Clin Sci (Lond) 2004;107:485-495.
    • (2004) Clin Sci (Lond) , vol.107 , pp. 485-495
    • Mischak, H.1    Kaiser, T.2    Walden, M.3    Hillmann, M.4
  • 51
    • 33344479181 scopus 로고    scopus 로고
    • Discovery and validation of new protein biomarkers for urothelial cancer: A prospective analysis
    • Theodorescu D, Wittke S, Ross MM, Walden M, et al: Discovery and validation of new protein biomarkers for urothelial cancer: a prospective analysis. Lancet Oncol 2006;7:230-240.
    • (2006) Lancet Oncol , vol.7 , pp. 230-240
    • Theodorescu, D.1    Wittke, S.2    Ross, M.M.3    Walden, M.4
  • 52
    • 27944451098 scopus 로고    scopus 로고
    • Combined top-down and bottom-up mass spectrometric approach to characterization of biomarkers for renal disease
    • Chalmers MJ, Mackay CL, Hendrickson CL, Wittke S, et al: Combined top-down and bottom-up mass spectrometric approach to characterization of biomarkers for renal disease. Anal Chem 2005; 77:7163-7171.
    • (2005) Anal Chem , vol.77 , pp. 7163-7171
    • Chalmers, M.J.1    Mackay, C.L.2    Hendrickson, C.L.3    Wittke, S.4
  • 53
    • 33745335841 scopus 로고    scopus 로고
    • Biomarker discovery by CE-MS enables sequence analysis via MS/MS with platform-independent separation
    • Zurbig P, Renfrow MB, Schiffer E, Novak J, et al: Biomarker discovery by CE-MS enables sequence analysis via MS/MS with platform-independent separation. Electrophoresis 2006;27:2111-2125.
    • (2006) Electrophoresis , vol.27 , pp. 2111-2125
    • Zurbig, P.1    Renfrow, M.B.2    Schiffer, E.3    Novak, J.4
  • 54
    • 0028180112 scopus 로고
    • Human hemofiltrate as a source of circulating bioactive peptides: Determination of amino acids, peptides and proteins
    • Schepky AG, Bensch KW, Schulz-Knappe P, Forssmann WG: Human hemofiltrate as a source of circulating bioactive peptides: determination of amino acids, peptides and proteins. Biomed Chromatogr 1994;8:90-94.
    • (1994) Biomed Chromatogr , vol.8 , pp. 90-94
    • Schepky, A.G.1    Bensch, K.W.2    Schulz-Knappe, P.3    Forssmann, W.G.4
  • 55
    • 0018210612 scopus 로고
    • Preparative isolation of middle molecular weight fractions from the hemofiltrate of patients with chronic uremia
    • Brunner H, Mann H, Essers U, Schultheis R, et al: Preparative isolation of middle molecular weight fractions from the hemofiltrate of patients with chronic uremia. Artif Organs 1978;2:375-377.
    • (1978) Artif Organs , vol.2 , pp. 375-377
    • Brunner, H.1    Mann, H.2    Essers, U.3    Schultheis, R.4
  • 56
    • 0030746097 scopus 로고    scopus 로고
    • Peptide bank generated by large-scale preparation of circulating human peptides
    • Schulz-Knappe P, Schrader M, Standker L, Richter R, et al: Peptide bank generated by large-scale preparation of circulating human peptides. J Chromatogr A 1997;776;125-132.
    • (1997) J Chromatogr A , vol.776 , pp. 125-132
    • Schulz-Knappe, P.1    Schrader, M.2    Standker, L.3    Richter, R.4
  • 57
    • 0343924648 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionisation mass spectrometry guided purification of human guanylin from blood ultrafiltrate
    • Schrader M, Jurgens M, Hess R, Schulz-Knappe P, et al: Matrix-assisted laser desorption/ionisation mass spectrometry guided purification of human guanylin from blood ultrafiltrate. J Chromatogr A 1997;776:139-145.
    • (1997) J Chromatogr A , vol.776 , pp. 139-145
    • Schrader, M.1    Jurgens, M.2    Hess, R.3    Schulz-Knappe, P.4
  • 58
    • 13444291499 scopus 로고    scopus 로고
    • Identification and characterization of novel endogenous proteolytic forms of the human angiogenesis inhibitors restin and endostatin
    • John H, Radtke K, Standker L, Forssmann WG: Identification and characterization of novel endogenous proteolytic forms of the human angiogenesis inhibitors restin and endostatin. Biochim Biophys Acta 2005;1747:161-170.
    • (2005) Biochim Biophys Acta , vol.1747 , pp. 161-170
    • John, H.1    Radtke, K.2    Standker, L.3    Forssmann, W.G.4
  • 59
    • 15444374044 scopus 로고    scopus 로고
    • Isolation and characterization of a novel proopiomelanocortin-derived peptide from hemofiltrate of chronic renal failure patients
    • Fricke K, Schulz A, John H, Forssmann WG, Maronde E: Isolation and characterization of a novel proopiomelanocortin-derived peptide from hemofiltrate of chronic renal failure patients. Endocrinology 2005;146:2060-2068.
    • (2005) Endocrinology , vol.146 , pp. 2060-2068
    • Fricke, K.1    Schulz, A.2    John, H.3    Forssmann, W.G.4    Maronde, E.5
  • 60
    • 0037084079 scopus 로고    scopus 로고
    • An automated on-line multidimensional HPLC system for protein and peptide mapping with integrated sample preparation
    • Wagner K, Miliotis T, Marko-Varga G, Bischoff R, Unger KK: An automated on-line multidimensional HPLC system for protein and peptide mapping with integrated sample preparation. Anal Chem 2002;74:809-820.
    • (2002) Anal Chem , vol.74 , pp. 809-820
    • Wagner, K.1    Miliotis, T.2    Marko-Varga, G.3    Bischoff, R.4    Unger, K.K.5
  • 61
    • 3142542638 scopus 로고    scopus 로고
    • A proteomic analysis of proteins removed by ultrafiltration during extracorporeal renal replacement therapy; in Thongboonkerd V, Klein JB (eds): Proteomics in Nephrology
    • Basel, Karger
    • Ward RA, Brinkley KA: A proteomic analysis of proteins removed by ultrafiltration during extracorporeal renal replacement therapy; in Thongboonkerd V, Klein JB (eds): Proteomics in Nephrology. Contrib Nephrol. Basel, Karger, 2004, vol 141, pp 280-291.
    • (2004) Contrib Nephrol , vol.141 , pp. 280-291
    • Ward, R.A.1    Brinkley, K.A.2
  • 63
    • 11144302513 scopus 로고    scopus 로고
    • Identification of proteins in slow continuous ultrafiltrate by reversed-phase chromatography and proteomics
    • Lefler DM, Pafford RG, Black NA, Raymond JR, Arthur JM: Identification of proteins in slow continuous ultrafiltrate by reversed-phase chromatography and proteomics. J Proteome Res 2004; 3:1254-1260.
    • (2004) J Proteome Res , vol.3 , pp. 1254-1260
    • Lefler, D.M.1    Pafford, R.G.2    Black, N.A.3    Raymond, J.R.4    Arthur, J.M.5
  • 65
    • 10744229731 scopus 로고    scopus 로고
    • Capillary electrophoresis coupled to mass spectrometry to establish polypeptide patterns in dialysis fluids
    • Kaiser T, Hermann A, Kielstein JT, Wittke S, et al: Capillary electrophoresis coupled to mass spectrometry to establish polypeptide patterns in dialysis fluids. J Chromatogr A 2003;1013:157-171.
    • (2003) J Chromatogr A , vol.1013 , pp. 157-171
    • Kaiser, T.1    Hermann, A.2    Kielstein, J.T.3    Wittke, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.